Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.2.29 - thymine-DNA glycosylase and Organism(s) Mus musculus

for references in articles please use BRENDA:EC3.2.2.29
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.29 thymine-DNA glycosylase
IUBMB Comments
Thymine-DNA glycosylase is part of the DNA-repair machinery. Thymine removal is fastest when it is from a G/T mismatch with a 5'-flanking C/G pair. The glycosylase removes uracil from G/U, C/U, and T/U base pairs faster than it removes thymine from G/T .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
Hydrolyses mismatched double-stranded DNA and polynucleotides, releasing free thymine.
Synonyms
thymine dna glycosylase, thymine-dna glycosylase, mismatch-specific thymine-dna glycosylase, pa-mig, g/t glycosylase, thymine dna-glycosylase, uracil/thymine dna glycosylase, mismatch-specific thymine-dna n-glycosylase, t:g mismatch-specific thymidine-dna glycosylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T/U mismatch DNA glycosylase
-
-
T:G mismatch-specific thymidine-DNA glycosylase
-
-
thymine DNA glycosylase
-
-
SYSTEMATIC NAME
IUBMB Comments
thymine-DNA deoxyribohydrolase (thymine-releasing)
Thymine-DNA glycosylase is part of the DNA-repair machinery. Thymine removal is fastest when it is from a G/T mismatch with a 5'-flanking C/G pair. The glycosylase removes uracil from G/U, C/U, and T/U base pairs faster than it removes thymine from G/T [3].
CAS REGISTRY NUMBER
COMMENTARY hide
149565-68-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
show the reaction diagram
additional information
?
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AP1
-
TDG activity is stimulated by APE1
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
low catalytic turnover of TDG
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
cellular TDG demonstrates PMA-dependent alterations in apparent molecular weight and isoelectric point
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
proliferating regions of the fetal bone
Manually annotated by BRENDA team
-
fetal, high expression
Manually annotated by BRENDA team
-
TDG transcripts are uniformly and ubiquitously expressed from 7.5 days post-coitum, but are then markedly enriched in specific tissues of the developing fetus. At 14.5 gestational days, TDG is strongly expressed in the developing nervous system, thymus, lung, liver, kidney and intestine. At later stages, high levels of expression were detected in the thymus, brain, nasal epithelium and within proliferating regions of the intestine, skin, kidney, teeth and bone
Manually annotated by BRENDA team
-
proliferating regions of the fetal intestine
Manually annotated by BRENDA team
-
proliferating regions of the fetal kidney
Manually annotated by BRENDA team
-
fetal, high expression
Manually annotated by BRENDA team
-
EC cell
Manually annotated by BRENDA team
-
proliferating regions of the fetal skin
Manually annotated by BRENDA team
-
fetal, high expression
Manually annotated by BRENDA team
-
proliferating regions of the fetal teeth
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
before germinal vesicle breakdown the enzyme is released from the nucleus into the cytoplasm
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
-
opposing roles of CBP/p300 and PKCalpha in regulating the DNA repair functions of TDG, the interplay of acetylation and phosphorylation of TDG in vivo may be critically important in the maintenance of CpG dinucleotides and epigenetic regulation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TDG_MOUSE
421
0
46879
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
cellular TDG demonstrates PMA-dependent alterations in apparent molecular weight and isoelectric point
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
-
TDG lysines are acetylated by CREB-binding protein, CBP, and p300. Acetylation of the N-terminal region abrogates high-affinity DNA binding and selectively prevents processing of G:T mispairs. TDG acetylation and phosphorylation are mutually exclusive, and their interplay dramatically alters the DNA mispair-processing functions of TDG
phosphoprotein
-
protein kinase C alpha interacts with TDG and phosphorylates N-terminal serine residues adjacent to lysines acetylated by CREB-binding protein, CBP, and p300. TDG acetylation and phosphorylation are mutually exclusive, and their interplay dramatically alters the DNA mispair-processing functions of TDG. Phosphorylation does not markedly alter DNA interactions, but may preserve G:T processing in vivo by preventing CBP-mediated acetylation
additional information
-
TDG catalytic efficiency of the protein is increased by SUMOylation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from NIH3T3 fibroblasts
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in mismatch-transfected B16F10 cells
-
expression in NIH3T3 fibroblasts
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, J.; Blue, E.K.; Hu, G.; Herring, B.P.
Thymine DNA glycosylase represses myocardin-induced smooth muscle cell differentiation by competing with serum response factor for myocardin binding.
J. Biol. Chem.
283
35383-35392
2008
Mus musculus
Manually annotated by BRENDA team
Li, Y.Q.; Zhou, P.Z.; Zheng, X.D.
Walsh, C.P.; Xu, G.L.: Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair
Nucleic Acids Res.
35
390-400
2007
Mus musculus
Manually annotated by BRENDA team
Niederreither, K.; Harbers, M.; Chambon, P.; Dolle, P.
Expression of T:G mismatch-specific thymidine-DNA glycosylase and DNA methyl transferase genes during development and tumorigenesis
Oncogene
17
1577-1585
1998
Mus musculus
Manually annotated by BRENDA team
Li, S.; Huang, Q.; Wang, L.; Lan, Y.; Zhang, X.; Yang, B.; Du, P.; Hua, Z.
A convenient spectrometric assay system for intracellular quantitative measurement of DNA glycosylase activity
Acta Biochim. Biophys. Sin. (Shanghai)
42
381-387
2010
Mus musculus
Manually annotated by BRENDA team
Mohan, R.D.; Litchfield, D.W.; Torchia, J.; Tini, M.
Opposing regulatory roles of phosphorylation and acetylation in DNA mispair processing by thymine DNA glycosylase
Nucleic Acids Res.
38
1135-1148
2010
Mus musculus
Manually annotated by BRENDA team
Visnes, T.; Doseth, B.; Pettersen, H.; Hagen, L.; Sousa, M.; Akbari, M.; Otterlei, M.; Kavli, B.; Slupphaug, G.; Krokan, H.
Uracil in DNA and its processing by different DNA glycosylases
Philos. Trans. R. Soc. Lond. B Biol. Sci.
364
563-568
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Ma, J.Y.; Zhao, K.; OuYang, Y.C.; Wang, Z.B.; Luo, Y.B.; Hou, Y.; Schatten, H.; Shen, W.; Sun, Q.Y.
Exogenous thymine DNA glycosylase regulates epigenetic modifications and meiotic cell cycle progression of mouse oocytes
Mol. Hum. Reprod.
21
186-194
2015
Mus musculus
Manually annotated by BRENDA team